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Proteins tend to bury hydrophobic residues inside their core during thefolding process to provide stability to the protein structure and to preventaggregation. Nevertheless, proteins do expose some 'sticky' hydrophobicresidues to the solvent. These residues can play an important functional role,for example in protein-protein and membrane interactions. Here, we investigatehow hydrophobic protein surfaces are by providing three measures for surfacehydrophobicity: the total hydrophobic surface area, the relative hydrophobicsurface area, and - using our MolPatch method - the largest hydrophobic patch.Secondly, we analyse how difficult it is to predict these measures fromsequence: by adapting solvent accessibility predictions from NetSurfP2.0, weobtain well-performing prediction methods for the THSA and RHSA, whilepredicting LHP is more difficult. Finally, we analyse implications of exposedhydrophobic surfaces: we show that hydrophobic proteins typically have lowexpression, suggesting cells avoid an overabundance of sticky proteins.

How sticky are our proteins? Quantifying hydrophobicity of the human proteome